Document Detail


Natural and Synthetic Inhibitors Binding to Human Heat Shock Protein 90 and Their Clinical Application.
MedLine Citation:
PMID:  22123555     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
This review describes the recent progress in the field of heat shock protein 90 (Hsp90) inhibitor design. Hsp90 is a heat shock protein with a molecular weight of approximately 90 kDa. Hsp90 is considered a good anticancer target because its inhibition leads to inactivation of its numerous client proteins participating in various signaling and other processes involved in cancer progression. Numerous Hsp90 inhibitors-leads currently tested in clinical trials are presented in this review. Furthermore, this review emphasizes the application of biophysical binding assays in the development of Hsp90 inhibitors. The binding of designed lead compounds to various Hsp90 constructs is measured by isothermal titration calorimetry and thermal shift assay. These assays provide a detailed energetic insight of the binding reaction, including the enthalpy, entropy, heat capacity, and the Gibbs free energy. A detailed description of the binding energetics helps to extend our knowledge of structure-activity relationships in the design of more potent inhibitors. The most active compounds are then tested for their absorption, distribution, metabolism, elimination, toxicity, and activity against cancer cell lines.
Authors:
Vilma Petrikaitė; Daumantas Matulis
Related Documents :
19233635 - Probing the recognition specificity of a protein molecularly imprinted polymer using fo...
21831265 - Ss-tea: entropy based identification of receptor specific ligand binding residues from ...
21739945 - Recognition properties of acyclic glycoluril oligomers.
17655295 - Allosterically regulated supramolecular catalysis of acyl transfer reactions for signal...
23968995 - Multispectroscopic methods reveal different modes of interaction of anti cancer drug mi...
11895445 - Lipopolysaccharide regions involved in the activation of escherichia coli outer membran...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-11-18
Journal Detail:
Title:  Medicina (Kaunas, Lithuania)     Volume:  47     ISSN:  1648-9144     ISO Abbreviation:  -     Publication Date:  2011 Nov 
Date Detail:
Created Date:  2011-11-29     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9425208     Medline TA:  Medicina (Kaunas)     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Institute of Biotechnology, Vilnius University, V. A. Graičiūno 8, 02241 Vilnius, Lithuania. vilma.petrikaite@bti.vu.lt.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Venomous Snakebites.
Next Document:  Assessment of Reliability in Isokinetic Testing Among Adolescent Basketball Players.